User:Charlotte Dietschy/Sandbox 1486
From Proteopedia
(Difference between revisions)
(New page: ==Your Heading Here (maybe something like 'Structure')== <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for you...) |
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==Your Heading Here (maybe something like 'Structure')== | ==Your Heading Here (maybe something like 'Structure')== | ||
| - | <StructureSection load=' | + | <StructureSection load='6fin' size='340' side='right' caption='Caption for this structure' scene=''> |
This is a default text for your page '''Charlotte Dietschy/Sandbox 1486'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page '''Charlotte Dietschy/Sandbox 1486'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
| + | 6FIN, also called DDR1 (Discodein Domain Receptor 1), is a receptor of the collagen. | ||
== Function == | == Function == | ||
| - | + | 6 FIN is part of the RTKs family (Receptor Tyrosyne Kinases) which play a key role in the communication of cells with their microenvironment. These molecules are involved in the regulation of cell growth, differentiation and metabolism. The protein encoded by this gene is a RTK that is widely expressed in normal and transformed epithelial cells and is activated by various types of collagen. | |
| + | 6FIN is a transferase, so it is an Enzym which catalyses the transfer reaction of a functional group from a donor molecule to an acceptor one. | ||
| + | Thé inhibition of this protein | ||
== Disease == | == Disease == | ||
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== Structural highlights == | == Structural highlights == | ||
| - | The DDR1 is a protein of 78.1kDa, it is formed of 6 principle | + | The DDR1 is a protein of 78.1kDa, it is formed of 6 principle α-helix. This protein can bind to 7 ions iodure and a molecule 3-[(3-cyclopropyl-1,2,4-oxadiazol-5-yl)methyl]-8-(1H-indazole-5-carbonyl)-1-phenyl-1,3,8-triazaspiro[4.5]decan-4-one. |
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
Revision as of 14:50, 10 January 2019
Your Heading Here (maybe something like 'Structure')
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
